Endocytosis Via Caveolae

Pelkmans, Lucas; Helenius, Ari

doi:10.1034/j.1600-0854.2002.30501.x

Cited by 668 publications

(513 citation statements)

References 105 publications

(160 reference statements)

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“…10 It is known that, in addition to the plasma membrane, Cavs are present in the transGolgi network, in caveosomes, as secreted proteins when it is phosphorylated in S 80 in response to different stresses. 36 However, the precise localization of P-Cav-1 is not clear, and it has been detected in focal adhesions, colocal- After that, they were stimulated with a combination of 20 ng/ml TNF-␣ and 20 ng/ml IL-1␤ for 1 hour. Total cellular extracts were prepared, and the amounts of Cav-1 and Y 14 -P-Cav-1 were analyzed by a western blot.…”

Section: Discussionmentioning

confidence: 99%

Dispensability and dynamics of caveolin-1 during liver regeneration and in isolated hepatic cells

et al. 2007

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C aveolae were originally identified with an electron microscope as flask-shaped membrane invaginations on the surface of epithelial 1 and endothelial cells. 2 These plasmalemmal vesicles are enriched in sphingolipids, cholesterol, and caveolin (Cav), the major protein constituent of these structures. 3 Three Cavs have been identified in differentiated cells with specific patterns of distribution. Cav-1 and Cav-2 are found in adipocytes and endothelial cells, 4 whereas Cav-3 is selectively expressed in muscle cells. 5 Caveolae participate in many cellular processes, including vesicular transport, 6 cholesterol homeostasis, 7 regulation of signal transduction, 8 integrin signaling, 9 and cell growth. 10 Despite this, it is rather surprising that all Cav-null mice are viable, including the complete caveola-less mouse; however, the combined loss of Cav-1 and Cav-3 has profound effects on the cardiovascular function. 11 Caveolae have now been demonstrated to concentrate a wide variety of signaling molecules, including Src family tyrosine kinases, H-Ras, heterotrimeric G protein ␣ subunits, protein kinase C isoforms, and endothelial nitric oxide synthase (NOS; i.e., NOS-3). 12 Many signaling molecules directly interact with Cav-1 through a defined modular protein domain, which is known as the Cavscaffolding domain. The Cav-scaffolding domain has been shown to directly inhibit the activation of NOS-3, 13 epidermal growth factor receptor, 14 and c-neu 15 among other molecules. Moreover, Cav-1 is a potent inhibitor of proliferative pathways such as the Ras-p42/p44 MAP (mitogen activated protein kinase) kinase cascades. 16 Cav-1 expression negatively regulates cell cycle progression through a p53/p21-dependent pathway, 17 and several cellular oncoproteins down-regulate Cav-1 expression. 10

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Section: Discussionmentioning

confidence: 99%

Dispensability and dynamics of caveolin-1 during liver regeneration and in isolated hepatic cells

et al. 2007

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“…Surface receptors in which trafficking to the membrane has been reported to be dependent on caveolin function include, but are not limited to, the D1 dopamine receptor [46], M1 muscarinic receptor [47], angiotensin II type 1 receptor [48], and glucagon-like peptide 1 receptor [49]. Notably, caveolins also play a role in receptor endocytosis [47,[50][51][52][53][54] providing an additional regulatory mechanism to modulate cell signaling. Caveolin-dependent endocytosis is a mechanism involving internalization of membrane components within caveolae resulting in the diminution of function.…”

Section: Caveolins: Important For the Trafficking And Clustering Of Mmentioning

confidence: 99%

Caveolin proteins and estrogen signaling in the brain

Luoma

Boulware

Mermelstein

2008

Molecular and Cellular Endocrinology

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Best described outside the nervous system, caveolins are structural proteins that form caveolae, functional microdomains at the plasma membrane that cluster related signaling molecules. Caveolin associated proteins include G protein coupled receptors and G proteins, receptor tyrosine kinases, as well as protein kinases, ion channels and various other signaling enzymes. Not surprisingly, a wide array of biological disorders are thought to be rooted in caveolin dysfunction. In addition, caveolins also traffic and cluster estrogen receptors to caveolae. Interactions between the estrogen receptors ERα and ERβ with caveolins appear critical in many non-neuronal cell types, e.g. disruption of normal function may underlie many forms of breast cancer. Recent findings suggest caveolins may also play an essential role in membrane estrogen receptor function in the nervous system. Not only are they expressed in neurons and glia, but different caveolin isoforms also appear necessary to generate distinct functional signaling complexes. With membrane estrogen receptors responsible for the efficient activation of a multitude of intracellular signaling pathways, which in turn influence a wide variety of nervous system functions, caveolin proteins are poised to act as the central coordinators of these processes.

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“…Clathrin-dependent endocytosis occurs constitutively in all known eukaryotic cells, defined by a requirement for clathrin and adaptor proteins to form the endocytic vesicle coat [2]. One of the most important clathrin-independent pathways is mediated by caveolae, which are flask-shaped plasma membrane invaginations marked by the presence of caveolin-1 [1,4]. Understanding the mechanism of different endocytic pathways and how these pathways are regulated is of critical importance in the study of cell signaling process, especially for transforming growth factor-β (TGF-β) sig-npg www.cell-research.com | Cell Research naling, where TGF-β receptors harness both clathrin-and caveolae-dependent pathways for internalization [5][6][7][8].…”

Section: Introductionmentioning

confidence: 99%

Internalization of the TGF-β type I receptor into caveolin-1 and EEA1 double-positive early endosomes

Yan

et al. 2015

Cell Res

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Endocytosis and intracellular sorting of transforming growth factor-β (TGF-β) receptors play an important regulatory role in TGF-β signaling. Two major endocytic pathways, clathrin-and caveolae-mediated endocytosis, have been reported to independently mediate the internalization of TGF-β receptors. In this study, we demonstrate that the clathrin-and caveolae-mediated endocytic pathways can converge during TGF-β receptor endocytic trafficking. By tracking the intracellular dynamics of fluorescently-labeled TGF-β type I receptor (TβRI), we found that after mediating TβRI internalization, certain clathrin-coated vesicles and caveolar vesicles are fused underneath the plasma membrane, forming a novel type of caveolin-1 and clathrin double-positive vesicles. Under the regulation of Rab5, the fused vesicles are targeted to early endosomes and thus deliver the internalized TβRI to the caveolin-1 and EEA1 double-positive early endosomes (caveolin-1-positive early endosomes). We further showed that the caveolin-1-positive early endosomes are positive for Smad3/SARA, Rab11 and Smad7/Smurf2, and may act as a multifunctional device for TGF-β signaling and TGF-β receptor recycling and degradation. Therefore, these findings uncover a novel scenario of endocytosis, the direct fusion of clathrin-coated and caveolae vesicles during TGF-β receptor endocytic trafficking, which leads to the formation of the multifunctional sorting device, caveolin-1-positive early endosomes, for TGF-β receptors.

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Endocytosis Via Caveolae

Cited by 668 publications

References 105 publications

Dispensability and dynamics of caveolin-1 during liver regeneration and in isolated hepatic cells

Dispensability and dynamics of caveolin-1 during liver regeneration and in isolated hepatic cells

Caveolin proteins and estrogen signaling in the brain

Internalization of the TGF-β type I receptor into caveolin-1 and EEA1 double-positive early endosomes

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